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THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 290, NO. three, pp. 1319 ?331, January 16, 2015 ?2015 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.Involvement of the Na /Ca2 exchanger isoform 1 (NCX1) in Neuronal Growth Element (NGF)-induced Neuronal Differentiation by means of Ca2 -dependent Akt PhosphorylationReceived for publication, July 7, 2014, and in revised form, November 21, 2014 Published, JBC Papers in Press, November 21, 2014, DOI 10.1074/jbc.M114.Agnese Secondo1, Alba Esposito1, Rossana Sirabella?, Francesca Boscia, Anna Pannaccione, Pasquale Molinaro, Maria Cantile, Roselia Ciccone, Maria Jos?Sisalli, Antonella Scorziello, Gianfranco Di Renzo, and Lucio Annunziato? In the Department of Neuroscience and Reproductive and Odontostomatological Sciences, School of Medicine, “Federico II” University of Naples, By way of Sergio Pansini 5, Naples 80131, Italy plus the �Fondazione Istituto di Ricovero e Cura a Carattere Scientifico (IRCCS) SDN, Naples 80143, ItalyBackground: NCX1 regulates intracellular Ca2 and Na homeostasis in neurons. Results: The NPY Y5 receptor Antagonist Molecular Weight overexpression of NCX1 induced neuronal differentiation through Akt as well as NGF exposure. NCX1 knockdown prevented NGF-induced neurite outgrowth. Conclusion: NCX1 participates in neuronal differentiation by ionic regulation and Akt phosphorylation. Significance: Learning how NCX1 participates in neurite outgrowth will boost the expertise of neuronal differentiation. NGF induces neuronal differentiation by modulating [Ca2 ]i. Having said that, the function with the 3 isoforms of your main Ca2 -extruding system, the Na /Ca2 exchanger (NCX), in NGF-induced differentiation remains unexplored. We investigated irrespective of whether NCX1, NCX2, and NCX3 isoforms could play a relevant function in neuronal differentiation by means of the modulation of [Ca2 ]i as well as the Akt pathway. NGF caused progressive neurite elongation; a important raise in the well-known marker of development cones, GAP-43; and an enhancement of endoplasmic reticulum (ER) Ca2 content and of Akt phosphorylation through an early activation of ERK1/2. Interestingly, through NGF-induced differentiation, the NCX1 protein level increased, NCX3 decreased, and NCX2 remained unaffected. In the very same time, NCX total activity increased. Furthermore, NCX1 colocalized and coimmunoprecipitated with GAP-43, and NCX1 silencing prevented NGF-induced effects on GAP-43 expression, Akt phosphorylation, and neurite outgrowth. However, the overexpression of its neuronal splicing isoform, NCX1.4, even within the absence of NGF, induced an increase in Akt phosphorylation and GAP-43 protein expression. Interestingly, tetrodotoxin-sensitive Na curren.